ID K2RPR0_MACPH Unreviewed; 619 AA.
AC K2RPR0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28 {ECO:0000256|ARBA:ARBA00040398};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28 {ECO:0000256|ARBA:ARBA00039685};
GN ORFNames=MPH_08042 {ECO:0000313|EMBL:EKG14767.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG14767.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG14767.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG14767.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBUNIT: Component of the U5 snRNP complex.
CC {ECO:0000256|ARBA:ARBA00038719}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000256|ARBA:ARBA00037954}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG14767.1}.
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DR EMBL; AHHD01000337; EKG14767.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RPR0; -.
DR STRING; 1126212.K2RPR0; -.
DR VEuPathDB; FungiDB:MPH_08042; -.
DR eggNOG; KOG0333; Eukaryota.
DR HOGENOM; CLU_003041_11_2_1; -.
DR InParanoid; K2RPR0; -.
DR OrthoDB; 5487240at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd17945; DEADc_DDX23; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF56; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW mRNA processing {ECO:0000256|ARBA:ARBA00023187};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 186..214
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 217..420
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 431..594
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..214
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 20..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 68785 MW; 3117165C6154CD81 CRC64;
MAPPPPPKPV AITQGGKPTA DKTGDKRQNP EDAERELIRQ RYMGSEQNTS TFSAKKKRKR
TTEKKFNFEW NAEEDTSTDY NPLYQTRAEA GFFGRGRLGG FSDDVVDNAT KRYVQALAER
DKEAGSVRAA EIMEMERRRK EEGGRAALDK HWSEKRLDQM RERDWRIFKE DFNISTKGGS
IPNPMRSWEE SGLPKRLLDI IKDVGYLEPS PIQRAAIPIA LGSRDLIGVA VTGSGKTAAF
LLPLLVYISE LPPLNEFTKN DGPYAIILAP TRELAQQIEI EAKKFATPLG FTCVSIVGGH
SIEEQAYNMR DGAEIIIATP GRLVDCIERR VLVLGQCCYV IMDEADRMID LGFEEPVNKI
LDALPVGNEK PDDETAENTV AMSQHLGGKD RYRQTMMYTA TMPPAVERIA RKYLRRPAIV
TIGNVGEAVE TVEQRVEFVS GEDKRKKRLQ EILNSGEFTP PIIVFVNIKR NCDAVARDIK
HMGFSSVTLH GSKTQEQREA ALASLRNGQV DVLVATDLAG RGIDVPDVSL VVNFNMATNI
ESYTHRIGRT GRAGKSGVAI TFLGNEDVDV MYDLKQMLSK SSISRVPEEL RKHEAAQQKR
SRGGNAKALD EGGKGGGMR
//
